A8FVT2

PR
Gene name
Ssed_2346
Protein name
Deoxyguanosinetriphosphate triphosphohydrolase-like protein
Names
Species
Shewanella sediminis (strain HAW-EB3)
KEGG Pathway
sse:Ssed_2346
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-51 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A8FVT2

Entry ID Method Resolution Chain Position Source
AF-A8FVT2-F1 Predicted AlphaFoldDB

No variants for A8FVT2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8FVT2

No associated diseases with A8FVT2

3 regional properties for A8FVT2

Type Name Position InterPro Accession
domain HD/PDEase domain 55 - 259 IPR003607
domain HD domain 59 - 250 IPR006674
domain Phosphohydrolase-associated domain 340 - 427 IPR026875

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
dGTPase activity Catalysis of the reaction: dGTP + H(2)O = 2'-deoxyguanosine + 2 H(+) + triphosphate.
magnesium ion binding Binding to a magnesium (Mg) ion.

1 GO annotations of biological process

Name Definition
dGTP catabolic process The chemical reactions and pathways resulting in the breakdown of dGTP, guanosine triphosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTESLWHERR LTEEKKRRND HRSPYQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
70 80 90 100 110 120
THSLEVSQIG TGIRAQLKQK RPEFDHLFDS MSLIESLCLA HDIGHPPFGH GGEVALNYMM
130 140 150 160 170 180
RDHGGFEGNG QTFRILTGLE PYTEYYGMNL CRRTLLGILK YPAPYSSLYR ASGNKPVNNI
190 200 210 220 230 240
RQLKPSQWTP VKGIFDDDSG ILDWVLEPLN GSDRERFLSH RDLGANKHLR TQFKSLDCSV
250 260 270 280 290 300
MELADDIAYA VHDLEDAIVM GIVTPSQWQQ DVASKLTLSH DAWIKEEFTN IGQNLFSHQH
310 320 330 340 350 360
HLRKDAIGTL VNGFVTAIDI VEDRAFTDPL LRFNAGLDTS FSEALEVLKQ FVYKYVIRKP
370 380 390 400 410 420
EIQMLEYKGQ QIVMELFEAF ESDPERLLPT HTQERWRESH TKGLNSHRVI ADYISGMTDE
430 440
FAARLHQHLF NPKAGSMIEL NGEL